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Granulocyte Colony-Stimulating Factor Upregulates the Vacuolar Proton ATPase in Human Neutrophils
Hans Niessen,
Grant W. Meisenholder,
Hai-Ling Li,
Stephen L. Gluck,
Beth S. Lee,
Barry Bowman,
Robert L. Engler,
Bernard M. Babior, and
Roberta A. Gottlieb
From the Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA; the Department of Medicine, Department of Veterans Affairs Medical Center, San Diego, CA; the Department of Medicine, Washington University School of Medicine, St Louis, MO; and the Department of Biology, University of California Santa Cruz, Santa Cruz, CA.
We have previously shown that granulocyte colony-stimulating factor (G-CSF ) delays spontaneous neutrophil apoptosis through activation of the vacuolar proton ATPase (v-ATPase). We have now examined the regulation of the v-ATPase in neutrophils exposed to G-CSF in vitro. When neutrophils were cultivated in the absence of G-CSF, the 57-kD cytosolic B subunit of the v-ATPase disappeared within 1 to 2 hours, its loss preceding the nuclear changes of apoptosis and coinciding with the onset of acidification. By contrast, in neutrophils cultured for 2 hours in the presence of G-CSF, the amount of the 57-kD subunit was similar to that in freshly isolated neutrophils. However, inhibition of protein synthesis with cycloheximide and actinomycin D led to loss of the 57-kD subunit even in the presence of G-CSF. These results indicated that ongoing protein synthesis was required to maintain the v-ATPase, and further suggested that G-CSF acted, at least in part, by maintaining synthesis of the 57-kD cytosolic subunit. G-CSF also promoted the translocation of the 57-and 33-kD cytosolic v-ATPase subunits to the membrane. Our findings suggested two coordinate mechanisms by which the activity of the v-ATPase could be increased by G-CSF: the synthesis of cytosolic v-ATPase subunits and their translocation to the membrane.
Blood, Vol. 90 No. 11 (December 1), 1997:
pp. 4598-4601
© 1997 by The American Society of Hematology.
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